Biology:D-alanine—D-alanine ligase
| D-Alanine—D-alanine ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.2.4 | ||||||||
| CAS number | 9023-63-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| D-ala D-ala ligase N-terminus | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 complex of y216f d-ala:d-ala ligase with adp and a phosphoryl phosphinate | |||||||||
| Identifiers | |||||||||
| Symbol | Dala_Dala_lig_N | ||||||||
| Pfam | PF01820 | ||||||||
| InterPro | IPR011127 | ||||||||
| SCOP2 | 2dln / SCOPe / SUPFAM | ||||||||
| |||||||||
| D-ala D-ala ligase C-terminus | |||||||||
|---|---|---|---|---|---|---|---|---|---|
complex of y216f d-ala:d-ala ligase with adp and a phosphoryl phosphinate | |||||||||
| Identifiers | |||||||||
| Symbol | Dala_Dala_lig_C | ||||||||
| Pfam | PF07478 | ||||||||
| Pfam clan | CL0179 | ||||||||
| InterPro | IPR011095 | ||||||||
| SCOP2 | 2dln / SCOPe / SUPFAM | ||||||||
| |||||||||
In enzymology, a D-alanine—D-alanine ligase (EC 6.3.2.4) is an enzyme that catalyzes the chemical reaction
- ATP + 2 D-alanine [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate + D-alanyl-D-alanine
Thus, the two substrates of this enzyme are ATP and D-alanine, whereas its 3 products are ADP, phosphate, and D-alanyl-D-alanine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is D-alanine:D-alanine ligase (ADP-forming). Other names in common use include alanine:alanine ligase (ADP-forming), and alanylalanine synthetase. This enzyme participates in d-alanine metabolism and peptidoglycan biosynthesis. Phosphinate and D-cycloserine are known to inhibit this enzyme.
The N-terminal region of the D-alanine—D-alanine ligase is thought to be involved in substrate binding, while the C-terminus is thought to be a catalytic domain.[1]
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1EHI, 1IOV, 1IOW, 2DLN, 2FB9, 2I80, 2I87, and 2I8C.
References
- ↑ "The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA)". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 8921–5. August 2000. doi:10.1073/pnas.150116497. PMID 10908650. Bibcode: 2000PNAS...97.8921R.
Further reading
- Ito, E; Strominger JL (1962). "Enzymatic synthesis of the peptide in bacterial uridine nucleotides II. Enzymatic synthesis and addition of D-alanyl-D-alanine". J. Biol. Chem. 237: 2696–2703. doi:10.1016/S0021-9258(19)73809-5.
- Neuhaus FC (1962). "Kinetic studies on D-Ala-D-Ala synthetase". Fed. Proc. 21: 229.
- van Heijenoort J (2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Nat. Prod. Rep. 18 (5): 503–19. doi:10.1039/a804532a. PMID 11699883.
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